Isoforms of Serratia marcescens nuclease. The role of Mg2+ in the hydrolysis mechanism.
Structural and functional differences between isoforms Sm1 and Sm2, a lack of influence of free Mg2+ on the isoform structures, formation of DNA-magnesium complex serving with great probability as a real substrate for the nuclease has been summarized on the basis of experimental data. Mg2+ forming a complex with phosphate groups of DNA are supposed to further increase the electrophilicity of the phosphorus atoms besides causing a conformational change of the substrate.
Filimonova
M N
MN
Department of Microbiology, Kazan State University, Russia. maria.filimonova@ksu.ru
Gubskaya
V P
VP
Nuretdinov
I A
IA
Benedik
M J
MJ
Bogomolnaya
L M
LM
Andreeva
M A
MA
Leshchinskaya
I B
IB
D002942:Circular Dichroism; D004247:DNA / Q000378:metabolism; D004706:Endodeoxyribonucleases / Q000378:metabolism*; D004722:Endoribonucleases / Q000378:metabolism*; D006868:Hydrolysis; D007526:Isoelectric Point; D007527:Isoenzymes / Q000378:metabolism; D007700:Kinetics; D008274:Magnesium / Q000378:metabolism*; D011487:Protein Conformation; D012706:Serratia marcescens / Q000201:enzymology*; D013329:Structure-Activity Relationship
D007527:Isoenzymes; D004247:DNA; D004706:Endodeoxyribonucleases; D004722:Endoribonucleases; C021835:Serratia marcescens nuclease; D008274:Magnesium